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Team:Valencia/Safety
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Our project does not raise safety issues in terms of researcher safety, public safety or environmental safety. Any of the new BioBrick parts that we have made this year (see SUBMITTED PARTS) raise any safety issue. | Our project does not raise safety issues in terms of researcher safety, public safety or environmental safety. Any of the new BioBrick parts that we have made this year (see SUBMITTED PARTS) raise any safety issue. | ||
| - | The prion that we have used in our project is extremely unlikely being pathogenic in humans and no such a case it has been registered in scientific literature. In fact, the infection of one organism with prions generated in another species frequently results in no disease. This effect received the name of “species barrier” and it has been clearly demonstrated that is closely related to the differences in prion protein sequence between donor and acceptor organisms. In some cases these differences are only in a few amino acids (Wickner et al., 2008). Specially, in the prion that we use in our project it has been observed the existence of a barrier to | + | The prion that we have used in our project is extremely unlikely being pathogenic in humans and no such a case it has been registered in scientific literature. In fact, the infection of one organism with prions generated in another species frequently results in no disease. This effect received the name of “species barrier” and it has been clearly demonstrated that is closely related to the differences in prion protein sequence between donor and acceptor organisms. In some cases these differences are only in a few amino acids (Wickner et al., 2008). Specially, in the prion that we use in our project it has been observed the existence of a barrier to its transmission (resulting from the formation of amyloid fibrils of the protein Sup35), between ''S. cerevisae'' and ''C. albicans''. The NH2-terminus prion-forming domain (PrD) of Sup35p from both species has a high N/Q content, associated with amyloid growth in several fungal yeasts (Wickner et al., 2008), but is extremely difficult for Sup35 amyloid of one species to initiate the conformational change in the other. Therefore the transmission of the prion from the yeast to humans, a species much less related, is absolutely impossible. |
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Safety
Our project does not raise safety issues in terms of researcher safety, public safety or environmental safety. Any of the new BioBrick parts that we have made this year (see SUBMITTED PARTS) raise any safety issue.
The prion that we have used in our project is extremely unlikely being pathogenic in humans and no such a case it has been registered in scientific literature. In fact, the infection of one organism with prions generated in another species frequently results in no disease. This effect received the name of “species barrier” and it has been clearly demonstrated that is closely related to the differences in prion protein sequence between donor and acceptor organisms. In some cases these differences are only in a few amino acids (Wickner et al., 2008). Specially, in the prion that we use in our project it has been observed the existence of a barrier to its transmission (resulting from the formation of amyloid fibrils of the protein Sup35), between S. cerevisae and C. albicans. The NH2-terminus prion-forming domain (PrD) of Sup35p from both species has a high N/Q content, associated with amyloid growth in several fungal yeasts (Wickner et al., 2008), but is extremely difficult for Sup35 amyloid of one species to initiate the conformational change in the other. Therefore the transmission of the prion from the yeast to humans, a species much less related, is absolutely impossible.
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